Defining the minimum size of a hydrophobic cluster in two-stranded alpha-helical coiled-coils: effects on protein stability.
D000409:Alanine / Q000737:chemistry / Q000235:genetics; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D002942:Circular Dichroism; D016384:Consensus Sequence; D030562:Databases, Protein; D006358:Hot Temperature; D057927:Hydrophobic and Hydrophilic Interactions; D007532:Isoleucine / Q000737:chemistry / Q000235:genetics; D007930:Leucine / Q000737:chemistry / Q000235:genetics; D008958:Models, Molecular; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry / Q000235:genetics; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000235:genetics; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014335:Tropomyosin / Q000737:chemistry / Q000235:genetics; D014461:Ultracentrifugation; D014508:Urea / Q000737:chemistry
D010455:Peptides; D011506:Proteins; D014335:Tropomyosin; D007532:Isoleucine; D014508:Urea; D007930:Leucine; D000409:Alanine